MISC

2008年8月

The impact of the 67 kDa laminin receptor on both cell-surface binding and anti-allergic action of tea catechins

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
  • Yoshinori Fujimura
  • ,
  • Daisuke Umeda
  • ,
  • Koji Yamada
  • ,
  • Hirofumi Tachibana

476
2
開始ページ
133
終了ページ
138
記述言語
英語
掲載種別
DOI
10.1016/j.abb.2008.03.002
出版者・発行元
ELSEVIER SCIENCE INC

Here, we investigated the structure-activity relationship of major green tea catechins and their corresponding epimers on cell-surface binding and inhibitory effect on histamine release. Galloylated catechins; (-)-epigallocatechin-3-O-gallate (EGCG), (-)-gallocatechin-3-O-gallate (GCG), (-)-epicatechin-3-O-gallate (ECG), and (-)-catechin-3-O-gallate (CG) showed the cell-surface binding to the human basophilic KU812 cells by surface plasmon resonance analysis, but their non-galloylated forms did not. Binding activities of pyrogallol-type catechins (EGCG and GCG) were higher than those of catechol-type catechins (ECG and CG). These patterns were also observed in their inhibitory effects on histamine release. Previously, we have reported that biological activities of EGCG are mediated through the binding to the cell-surface 67 kDa laminin receptor (67LR). Downregulation of 67LR expression caused a reduction of both activities of galloylated catechins. These results suggest that both the galloyl moiety and the B-ring hydroxylation pattern contribute to the exertion of biological activities of tea catechins and their 67LR-dependencies. (C) 2008 Elsevier Inc. All rights reserved.

Web of Science ® 被引用回数 : 43

リンク情報
DOI
https://doi.org/10.1016/j.abb.2008.03.002
CiNii Articles
http://ci.nii.ac.jp/naid/80019725178
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/18358230
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000258424500006&DestApp=WOS_CPL

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